Collaboration Teams When contributing to the reading guide, follow these steps: 1) First complete the reading guide on your own from the chemistry unit page.
2) Write your response to a question in word and then copy it. Be sure to upload pictures and/or video for each question.
3) Click on the edit button and then go to the appropriate question and paste your answer below it. Sign your contribution with your first name and last initial and TEAM COLOR
4) From the save dropdown menu choose "save with comment , place a summary of what you did and sign it (e.g. "I answered chp 26 question 3" - Tom S.) Then click Save.
Blue
Purple
Green
Yellow
Orange
Red
Sam Fernanda Ashley
Josh
Chris
Amy
Kelly
Mike
Alina
Dahlia
Ryan Alecia Taihlor
Brett Sam Katie
Tyler
Nikki
Megan
1-2, 15
3-5,16
6-8,17
9-10,18
11-12, 19
13-14, 20
Chapter 5 Guided Reading Assignment
1.Upload pictures/videos of a monomer, polymer, condensation reaction, and hydrolysis. Explain each with examples.
An example of hydrolysis within our bodies is our digestive system. An example of dehydration synthesis would be amino acids joining to peptide bonds to form proteins. -Ashley A.
2.What is a glycosidic linkage and what the numbers 1-4 and 1-2 relate to? A glycosidic linkage joins 2 monosaccharides to form a disaccharide. The linkage forms a covalent bond between the two monosaccharides by a dehydration reaction. The numbers refer to the number carbon that is being joined with another carbon. (1-4 would be the number 1 carbon bonded to the number 4 carbon), (1-2 is the number 1 carbon bonded to the number 2). Example #1: 1-4 linkage
The number 1 carbon on one glucose unit links to the number 4 carbon of another glucose unit to make maltose. (Most starches are 1-4 linkages)
Example #2: 1-2 linkage
The number 1 carbon in the glucose unit links with the number 2 carbon in the fructose unit to form sucrose.
-Ashley A.
3. Compare and contrast the two storage polysaccharides.
The two storage polysaccharides, starch and glycogen, are both made up entirely of glucose. Plants use starch while animals use glycogen. There are two types of starch: amylose, which is unbranched, and amylopectin, which is branched with 1-6 linkages at the branch points. Glycogen only has one type which is similar to amylopectin, yet more intricate in its branches.
Picture shows 3 types of storage polysaccharides. Josh Scheerer
4.Compare and contrast the two structural polysaccharides.
There are two structural polysaccharides, Cellulose and Chitin. Cellulose occurs in plants and Chitin occurs in arthropods and fungi. The two structural polysaccharides are alike because they both similar physical characteristics.
Picture shows both structure polysaccharides.
Josh Scheerer
5.Why are lipids grouped together as a family of molecules?
Lipids are grouped together because have hydrophobic tails. The tails of the lipids stay together and the heads block the water from reaching the tails. This results in the formation of micelles and bilayers.
Picture shows 1) lipid bilayer and 2) micelle. Josh Scheerer
6.What are the building blocks of fats and how do they combine?
The building blocks of fats are three fatty acids (has a carboxyl and a hydrocarbon) and one glycerol (is an alcohol with three carbons). They combine when one water molecule is removed for each fatty acid joined to the glycerol (Dehydration reaction).
Mike G.
7.Contrast saturated and unsaturated fats – how does this relate to the concept that structure and function (how they are used by living things) are linked
At room temperature the molecules of a saturated fat such as butter are packed closely together, forming a solid. At room temperature the molecules of an unsaturated fat, such as olive oil are not packed together closely enough to solidify because of the kinks and their faty acid tails. Saturated fats have no double bonds between the carbon atoms of the fatty acid chain and are fully saturated with hydrogen atoms. *They are unhealthy in regards to nutrition. An unsaturated fat occurs when there is at least one double bond within the fatty acid chain. This relates to the concept that structure and function are linked because; the type of fatty acid produced depends on the structure of the hydrocarbon chain of the fatty acid & according to the structure the fat will either be an unsaturated or a saturated fat each with its own unique properties.
-Dahlia M.
8. Upload a picture of a phospholipid and label significant functional groups.
There is a phosphate group in the hydrophilic head.
-Mike G.
9. How would you recognize a basic steroid molecule? a basic steroid molecule consists of four fused rings, three six-membered rings and one five-membered ring. Each steroid has a different functional group (noted in red on the picture below) that makes it different.
-Ryan H.
10. upload pictures of the eight types of proteins and their basic function. 1. Enzymatic protein- controls acceleration of chemical reactions 2. Structural protein-the cells structure 3. Storage protein-storage of amino acids 4. Transport protein-transportation of other substances 5. Hormonal protein-coordination of an organisms activities 6. Contractile and Motor protein-control movement
7. Defensive protein- protects against disease 8. Genetic protein-nucleic acid such as DNA and RNA
-Taihlor C.
11. What are the names for the monomers and polymers of proteins
Video of RNA Polymer of proteins are called polypeptide. Monomer of polypeptide is called an amino acid the sequence of these proteins of are called primary structures.
-Brett S. 12. Upload a video of the catalytic cycle of an enzyme – and then describe a real world example.
A real world example would be the idea of conversion of sucrose to glucose and fructose using the enzyme sucrase.
-Brett S. 13. upload pictures of two amino acids – note the amino group, the carboxyl group and the alpha carbon, circle the water molecule to be removed and then note the peptide bond formed when the two are joined.
two amino acids, when water is pulled through you get a peptide bond
-Nichole F
14. Explain the four levels of protein structure – Include pictures a.Primary The primary structure of a protein is inherited by genetic information unique sequence of amino acids.
b.Secondary It folds and curls in the polypeptide chain. It results from hydrogen bonds between the repeating constituents of the polypeptide backbone. There is a beta sheet and alpha helix.
c.Tertiary It is superimposed on the patterns of the secondary structure. The conformation of protein can be reinforced further by the covalent bonds called disulfide.
d.Quaternary It is protons that consist of two or more polypeptide chains aggregated into one functional macromolecule. The overall protein structure results from aggregation of these polypeptide subunits.
15. How does the characteristics of an amino acid – nonpolar, polar, acidic or basic relate to the issue of tertiary and quaternary structure?
In tertiary structure, the amino acid side chains (the "R" part of the amino acid) can affect tertiary structure in the following ways. If the end of the side chain is non-polar, the amino acid will gravitate towards the center of a protein chain in a process called hydrophobic reaction, along with the other non-polar amino acids. Then, van der Walls hold the structure in place. Conversely, if the end of a side chain is polar, it will bond with the water molecules outside the structure via hydrogen bonding. Another factor is the charge of a side chain. If a side chain is acidic (due to the carboxyl group dissociating and losing an H+ ion), it will become negative. If the side chain is basic (due to a base like NH2 picking up an H+ ion), it will become positive. The acidic and basic side chains will then form ionic bonds with their respective partners, adding more stability. Finally, side chains with sulfhydryl ends can form disulfide "bridges" to connect.
In quaternary structure, it is the polypeptide backbone that affects shape. The position of the polypeptide backbone based on the tertiary structure then affects the position of the fully assembled protein in quaternary structure based once again on polarity and pH.
-Sam Viknyansky BLUE (Sorry, I tried changing the font color but it didn't work)
The acidity and polarity of the amino acid side chains and the peptide backbone affect tertiary( top right) and quaternary (bottom right) structure.
16. What does denaturation mean and why is it important? Provide an everyday example. Denaturation is when the protein may unravel and lose it's native conformation due to the alterations to aspects of it's enviroment. It changes the structure of proteins, and therefore the way that they react. - Alina D.
Video shows the denaturation of protein in food. In the picture the Native state changes through denaturation, and the active Site is lost. Due to changes in environment, proteins may change to Denatured State. -Alina D.
17. What are chaperonins and what is their role in protein structure? Chaperonins are protein molecules that assist the proper folding of other proteins. Their role in protein structure includes helping to keep the new polypeptides segregated from bad influences in the cytoplasmic environment while it folds spontaneously.Chaperonins help with the protein folding problem.
Pathways of chaperone-mediated protein folding in the cytosol
-Dahlia M
.
18. Describe the technique of x-ray crystallography. It is a method used to determine a proteins 3 dimentional shape. Scientist aim the ray through the crystallized protien, the atoms are then deflected into a orderly array, which is exposed onto photographic film, producing a pattern of spots which they (the scientists) will read, to figure out the shape.
alecia seliga 19. What are the roles of nucleic acids
The role of nucleic acid is to allow molecules to enable its living organisms to reproduce their own complex components. The nucleic acid allows an organism to pass their genes along, and it will determine the features of a future organism. Nucleic acids include that of RNA and DNA. DNA sends instructions to assemble proteins from amino acids and RNA which is also a nucleic acid is a major role in creating proteins that are within the cell. Nucleic acids allow organisms to reproduce specific parts of DNA from one generation to the next. A new baby will inherit enough strong traits form mother and father to be able to survive.-Sam B.
Video for Nucleic acids DNA and RNA. Image of Nucleic acid
-Brett S.
20. Upload a picture of DNA that includes significant labels and explain what is meant by the term that DNA is antiparallel? The term antiparallel is referring to DNA’s double helix. DNA is comprised of the bases: cytosine, guanine, adenine, and thymine. These bases can only pair up one way AT or TA, GC or CG. When a cell nucleus splits, it strands into two antiparallel parts which will eventually be used in the new nucleus of a new cell. -Nichole f
When contributing to the reading guide, follow these steps:
1) First complete the reading guide on your own from the chemistry unit page.
2) Write your response to a question in word and then copy it. Be sure to upload pictures and/or video for each question.
3) Click on the edit button and then go to the appropriate question and paste your answer below it. Sign your contribution with your first name and last initial and TEAM COLOR
4) From the save dropdown menu choose "save with comment , place a summary of what you did and sign it (e.g. "I answered chp 26 question 3" - Tom S.) Then click Save.
Fernanda
Ashley
Chris
Amy
Kelly
Alina
Dahlia
Alecia
Taihlor
Sam
Katie
Nikki
Megan
Chapter 5 Guided Reading Assignment
1.Upload pictures/videos of a monomer, polymer, condensation reaction, and hydrolysis. Explain each with examples.
An example of hydrolysis within our bodies is our digestive system.
An example of dehydration synthesis would be amino acids joining to peptide bonds to form proteins.
-Ashley A.
2.What is a glycosidic linkage and what the numbers 1-4 and 1-2 relate to?
A glycosidic linkage joins 2 monosaccharides to form a disaccharide. The linkage forms a covalent bond between the two monosaccharides by a dehydration reaction. The numbers refer to the number carbon that is being joined with another carbon. (1-4 would be the number 1 carbon bonded to the number 4 carbon), (1-2 is the number 1 carbon bonded to the number 2).
Example #1: 1-4 linkage
The number 1 carbon on one glucose unit links to the number 4 carbon of another glucose unit to make maltose. (Most starches are 1-4 linkages)
Example #2: 1-2 linkage
The number 1 carbon in the glucose unit links with the number 2 carbon in the fructose unit to form sucrose.
-Ashley A.
3. Compare and contrast the two storage polysaccharides.
The two storage polysaccharides, starch and glycogen, are both made up entirely of glucose. Plants use starch while animals use glycogen. There are two types of starch: amylose, which is unbranched, and amylopectin, which is branched with 1-6 linkages at the branch points. Glycogen only has one type which is similar to amylopectin, yet more intricate in its branches.
Picture shows 3 types of storage polysaccharides.
Josh Scheerer
4.Compare and contrast the two structural polysaccharides.
There are two structural polysaccharides, Cellulose and Chitin. Cellulose occurs in plants and Chitin occurs in arthropods and fungi. The two structural polysaccharides are alike because they both similar physical characteristics.
Picture shows both structure polysaccharides.
Josh Scheerer
5.Why are lipids grouped together as a family of molecules?
Lipids are grouped together because have hydrophobic tails. The tails of the lipids stay together and the heads block the water from reaching the tails. This results in the formation of micelles and bilayers.
Picture shows 1) lipid bilayer and 2) micelle.
Josh Scheerer
6.What are the building blocks of fats and how do they combine?
The building blocks of fats are three fatty acids (has a carboxyl and a hydrocarbon) and one glycerol (is an alcohol with three carbons). They combine when one water molecule is removed for each fatty acid joined to the glycerol (Dehydration reaction).
Mike G.
7.Contrast saturated and unsaturated fats – how does this relate to the concept that structure and function (how they are used by living things) are linked
At room temperature the molecules of a saturated fat such as butter are packed closely together, forming a solid. At room temperature the molecules of an unsaturated fat, such as olive oil are not packed together closely enough to solidify because of the kinks and their faty acid tails. Saturated fats have no double bonds between the carbon atoms of the fatty acid chain and are fully saturated with hydrogen atoms.
*They are unhealthy in regards to nutrition.
An unsaturated fat occurs when there is at least one double bond within the fatty acid chain.
This relates to the concept that structure and function are linked because; the type of fatty acid produced depends on the structure of the hydrocarbon chain of the fatty acid & according to the structure the fat will either be an unsaturated or a saturated fat each with its own unique properties.
-Dahlia M.
8. Upload a picture of a phospholipid and label significant functional groups.
There is a phosphate group in the hydrophilic head.
-Mike G.
9. How would you recognize a basic steroid molecule?
a basic steroid molecule consists of four fused rings, three six-membered rings and one five-membered ring. Each steroid has a different functional group (noted in red on the picture below) that makes it different.
-Ryan H.
10. upload pictures of the eight types of proteins and their basic function.
1. Enzymatic protein-
controls acceleration of chemical reactions
2. Structural protein-the cells structure
3. Storage protein-storage of amino acids
4. Transport protein-transportation of other substances
5. Hormonal protein-coordination of an organisms activities
6. Contractile and Motor protein-control movement
7. Defensive protein- protects against disease
8. Genetic protein-nucleic acid such as DNA and RNA
-Taihlor C.
11. What are the names for the monomers and polymers of proteins
Video of RNA Polymer of proteins are called polypeptide. Monomer of polypeptide is called an amino acid the sequence of these proteins of are called primary structures.
-Brett S.12. Upload a video of the catalytic cycle of an enzyme – and then describe a real world example.
A real world example would be the idea of conversion of sucrose to glucose and fructose using the enzyme sucrase.
-Brett S.13. upload pictures of two amino acids – note the amino group, the carboxyl group and the alpha carbon, circle the water molecule to be removed and then note the peptide bond formed when the two are joined.
-Nichole F
14. Explain the four levels of protein structure – Include pictures
a.Primary
The primary structure of a protein is inherited by genetic information unique sequence of amino acids.
b.Secondary
It folds and curls in the polypeptide chain. It results from hydrogen bonds between the repeating constituents of the polypeptide backbone. There is a beta sheet and alpha helix.
c.Tertiary
It is superimposed on the patterns of the secondary structure. The conformation of protein can be reinforced further by the covalent bonds called disulfide.
d.Quaternary
It is protons that consist of two or more polypeptide chains aggregated into one functional macromolecule. The overall protein structure results from aggregation of these polypeptide subunits.
15. How does the characteristics of an amino acid – nonpolar, polar, acidic or basic relate to the issue of tertiary and quaternary structure?
In tertiary structure, the amino acid side chains (the "R" part of the amino acid) can affect tertiary structure in the following ways. If the end of the side chain is non-polar, the amino acid will gravitate towards the center of a protein chain in a process called hydrophobic reaction, along with the other non-polar amino acids. Then, van der Walls hold the structure in place. Conversely, if the end of a side chain is polar, it will bond with the water molecules outside the structure via hydrogen bonding. Another factor is the charge of a side chain. If a side chain is acidic (due to the carboxyl group dissociating and losing an H+ ion), it will become negative. If the side chain is basic (due to a base like NH2 picking up an H+ ion), it will become positive. The acidic and basic side chains will then form ionic bonds with their respective partners, adding more stability. Finally, side chains with sulfhydryl ends can form disulfide "bridges" to connect.
In quaternary structure, it is the polypeptide backbone that affects shape. The position of the polypeptide backbone based on the tertiary structure then affects the position of the fully assembled protein in quaternary structure based once again on polarity and pH.
-Sam Viknyansky BLUE (Sorry, I tried changing the font color but it didn't work)
16. What does denaturation mean and why is it important? Provide an everyday example.
Denaturation is when the protein may unravel and lose it's native conformation due to the alterations to aspects of it's enviroment. It changes the structure of proteins, and therefore the way that they react.
- Alina D.
Video shows the denaturation of protein in food.
In the picture the Native state changes through denaturation, and the active Site is lost. Due to changes in environment, proteins may change to Denatured State.
-Alina D.
17. What are chaperonins and what is their role in protein structure?
Chaperonins are protein molecules that assist the proper folding of other proteins. Their role in protein structure includes helping to keep the new polypeptides segregated from bad influences in the cytoplasmic environment while it folds spontaneously.Chaperonins help with the protein folding problem.
-Dahlia M
.
18. Describe the technique of x-ray crystallography.
It is a method used to determine a proteins 3 dimentional shape. Scientist aim the ray through the crystallized protien, the atoms are then deflected into a orderly array, which is exposed onto photographic film, producing a pattern of spots which they (the scientists) will read, to figure out the shape.
alecia seliga
19. What are the roles of nucleic acids
The role of nucleic acid is to allow molecules to enable its living organisms to reproduce their own complex components. The nucleic acid allows an organism to pass their genes along, and it will determine the features of a future organism. Nucleic acids include that of RNA and DNA. DNA sends instructions to assemble proteins from amino acids and RNA which is also a nucleic acid is a major role in creating proteins that are within the cell. Nucleic acids allow organisms to reproduce specific parts of DNA from one generation to the next. A new baby will inherit enough strong traits form mother and father to be able to survive.-Sam B.
Video for Nucleic acids DNA and RNA.
Image of Nucleic acid
-Brett S.
20. Upload a picture of DNA that includes significant labels and explain what is meant by the term that DNA is antiparallel?
The term antiparallel is referring to DNA’s double helix. DNA is comprised of the bases: cytosine, guanine, adenine, and thymine. These bases can only pair up one way AT or TA, GC or CG. When a cell nucleus splits, it strands into two antiparallel parts which will eventually be used in the new nucleus of a new cell.